NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW;
DOI=10.1007/s004380050409; PubMed=9108283 [NCBI, ExPASy, EBI, Israel, Japan]
Manna A.C., Das H.K.;
"Characterization and mutagenesis of the leucine biosynthetic genes of Azotobacter vinelandii: an analysis of the rarity of amino acid auxotrophs.";
Mol. Gen. Genet. 254:207-217(1997).

Comments

FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
CATALYTIC ACTIVITY: 3-carboxy-2-hydroxy-4-methylpentanoate + NAD⁺ = 3-carboxy-4-methyl-2-oxopentanoate + NADH.
COFACTOR: Binds 1 magnesium or manganese ion per subunit (By similarity).
PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y11280; CAA72151.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q56268; 1A05. [HSSP ENTRY / PDB]

ModBase

P96197.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003862;	Molecular function: 3-isopropylmalate dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0009098;	Biological process: leucine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01033; -; 1.
PBIL [Tree]

InterPro

IPR004429; 3-isopropylmalate_DHase.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.718.10; IDH_IMDH; 1.

PANTHER

PTHR11835; IDH_IMDH_dimeric; 1.
PTHR11835:SF13; IPMDH; 1.

Pfam

PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00169; leuB; 1.

PROSITE

PS00470; IDH_IMDH; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 360`	`360`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083631`
`METAL`	`223 223`		`Magnesium or manganese (By similarity).`
`METAL`	`247 247`		`Magnesium or manganese (By similarity).`
`METAL`	`251 251`		`Magnesium or manganese (By similarity).`
`BINDING`	`133 133`		`Substrate (By similarity).`
`BINDING`	`223 223`		`Substrate (By similarity).`
`SITE`	`140 140`	`1`	`Important for catalysis (By similarity).`
`SITE`	`191 191`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 360 AA [This is the length of the unprocessed precursor]

Molecular weight: 38974 Da [This is the MW of the unprocessed precursor]

CRC64: 16AAEC7966EDAC6A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKQILVLPG DGIGPEIMAE AVKVLQLANE KYQLGFVLGY DELGGAAVDK YGVPLADETL 

        70         80         90        100        110        120 
ERARRRCHPA RRRRRSEMGR HRPGHPPGAR PAENPFATGP VRQPAPGVLY PQLAEASTLR 

       130        140        150        160        170        180 
PEVVAGLDIL IVRELTGGIY FGAPRESRLL ANGERMAYDT LPYSESEIRR IAKVGFDMAR 

       190        200        210        220        230        240 
VRGKKLCSVD KANVLASSQL WRAVVEEVAK DYPDVVLSHM YVDNAAMQLV RAPKQFDVIV 

       250        260        270        280        290        300 
TDNMFGDILS DEASMLTGSI GMLPSASLDA DNKGMYEPCH GSRRPDIAGK GIANPLATIL 

       310        320        330        340        350        360 
SVSMMLRYSF GQVEAANAIE QAVSKVLDQG LRTGDIWSEG CRKVGTAEMG DAVVAALATL

P96197 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools